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P55157

- MTP_HUMAN

UniProt

P55157 - MTP_HUMAN

Protein

Microsomal triglyceride transfer protein large subunit

Gene

MTTP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the secretion of plasma lipoproteins that contain apolipoprotein B.

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. lipid transporter activity Source: Reactome

    GO - Biological processi

    1. cholesterol homeostasis Source: Ensembl
    2. lipid metabolic process Source: ProtInc
    3. lipoprotein metabolic process Source: Reactome
    4. lipoprotein transport Source: Ensembl
    5. protein lipidation Source: Ensembl
    6. response to calcium ion Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. triglyceride metabolic process Source: Ensembl

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_6841. Chylomicron-mediated lipid transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microsomal triglyceride transfer protein large subunit
    Gene namesi
    Name:MTTP
    Synonyms:MTP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:7467. MTTP.

    Subcellular locationi

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. brush border membrane Source: Ensembl
    3. endoplasmic reticulum lumen Source: Reactome
    4. Golgi apparatus Source: Ensembl
    5. membrane-bounded vesicle Source: Ensembl
    6. microvillus membrane Source: Ensembl
    7. receptor complex Source: MGI
    8. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Abetalipoproteinemia (ABL) [MIM:200100]: An autosomal recessive disorder of lipoprotein metabolism. Affected individuals produce virtually no circulating apolipoprotein B-containing lipoproteins (chylomicrons, VLDL, LDL, lipoprotein(A)). Malabsorption of the antioxidant vitamin E occurs, leading to spinocerebellar and retinal degeneration.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti540 – 5401R → H in ABL; loss of activity. 2 Publications
    VAR_010642
    Natural varianti590 – 5901S → I in ABL. 1 Publication
    VAR_010643
    Natural varianti746 – 7461G → E in ABL. 1 Publication
    VAR_010644
    Natural varianti780 – 7801N → Y in ABL; loss of activity. 1 Publication
    VAR_014019

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi540 – 5401R → K: No change of activity. 1 Publication
    Mutagenesisi878 – 8781C → S: Loss of activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi200100. phenotype.
    Orphaneti14. Abetalipoproteinemia.
    426. Familial hypobetalipoproteinemia.
    PharmGKBiPA164742099.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 894876Microsomal triglyceride transfer protein large subunitPRO_0000041593Add
    BLAST

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP55157.
    PaxDbiP55157.
    PRIDEiP55157.

    PTM databases

    PhosphoSiteiP55157.

    Expressioni

    Tissue specificityi

    Liver and small intestine. Also found in ovary, testis and kidney.1 Publication

    Inductioni

    Positively regulated by cholesterol and negatively regulated by insulin.1 Publication

    Gene expression databases

    ArrayExpressiP55157.
    BgeeiP55157.
    CleanExiHS_MTTP.
    GenevestigatoriP55157.

    Organism-specific databases

    HPAiHPA054862.

    Interactioni

    Subunit structurei

    Heterodimer composed of MTTP and of protein disulfide isomerase (P4HB/PDI).By similarity

    Protein-protein interaction databases

    BioGridi110641. 1 interaction.
    MINTiMINT-1537333.
    STRINGi9606.ENSP00000265517.

    Structurei

    3D structure databases

    ProteinModelPortaliP55157.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 659632VitellogeninPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 vitellogenin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG272516.
    HOGENOMiHOG000113688.
    HOVERGENiHBG006416.
    InParanoidiP55157.
    KOiK14463.
    PhylomeDBiP55157.
    TreeFamiTF328754.

    Family and domain databases

    Gene3Di1.25.10.20. 1 hit.
    2.30.230.10. 1 hit.
    InterProiIPR015819. Lipid_transp_b-sht_shell.
    IPR001747. Lipid_transpt_N.
    IPR015816. Vitellinogen_b-sht_N.
    IPR011030. Vitellinogen_superhlx.
    [Graphical view]
    PfamiPF01347. Vitellogenin_N. 1 hit.
    [Graphical view]
    SMARTiSM00638. LPD_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48431. SSF48431. 1 hit.
    SSF56968. SSF56968. 1 hit.
    PROSITEiPS51211. VITELLOGENIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55157-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MILLAVLFLC FISSYSASVK GHTTGLSLNN DRLYKLTYST EVLLDRGKGK    50
    LQDSVGYRIS SNVDVALLWR NPDGDDDQLI QITMKDVNVE NVNQQRGEKS 100
    IFKGKSPSKI MGKENLEALQ RPTLLHLIHG KVKEFYSYQN EAVAIENIKR 150
    GLASLFQTQL SSGTTNEVDI SGNCKVTYQA HQDKVIKIKA LDSCKIARSG 200
    FTTPNQVLGV SSKATSVTTY KIEDSFVIAV LAEETHNFGL NFLQTIKGKI 250
    VSKQKLELKT TEAGPRLMSG KQAAAIIKAV DSKYTAIPIV GQVFQSHCKG 300
    CPSLSELWRS TRKYLQPDNL SKAEAVRNFL AFIQHLRTAK KEEILQILKM 350
    ENKEVLPQLV DAVTSAQTSD SLEAILDFLD FKSDSSIILQ ERFLYACGFA 400
    SHPNEELLRA LISKFKGSIG SSDIRETVMI ITGTLVRKLC QNEGCKLKAV 450
    VEAKKLILGG LEKAEKKEDT RMYLLALKNA LLPEGIPSLL KYAEAGEGPI 500
    SHLATTALQR YDLPFITDEV KKTLNRIYHQ NRKVHEKTVR TAAAAIILNN 550
    NPSYMDVKNI LLSIGELPQE MNKYMLAIVQ DILRFEMPAS KIVRRVLKEM 600
    VAHNYDRFSR SGSSSAYTGY IERSPRSAST YSLDILYSGS GILRRSNLNI 650
    FQYIGKAGLH GSQVVIEAQG LEALIAATPD EGEENLDSYA GMSAILFDVQ 700
    LRPVTFFNGY SDLMSKMLSA SGDPISVVKG LILLIDHSQE LQLQSGLKAN 750
    IEVQGGLAID ISGAMEFSLW YRESKTRVKN RVTVVITTDI TVDSSFVKAG 800
    LETSTETEAG LEFISTVQFS QYPFLVCMQM DKDEAPFRQF EKKYERLSTG 850
    RGYVSQKRKE SVLAGCEFPL HQENSEMCKV VFAPQPDSTS SGWF 894
    Length:894
    Mass (Da):99,351
    Last modified:October 1, 1996 - v1
    Checksum:iB20260C136BDAB9F
    GO
    Isoform 2 (identifier: P55157-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-151: EFYSYQNEAVAIENIKRG → GRLDSTTFSPTSYFSSLQ
         152-894: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:151
    Mass (Da):16,865
    Checksum:iF0A042FD95FA8F3A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti585 – 5851F → L in CAA42200. (PubMed:8361539)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti95 – 951Q → H.1 Publication
    Corresponds to variant rs61733139 [ dbSNP | Ensembl ].
    VAR_014016
    Natural varianti98 – 981E → D.
    Corresponds to variant rs2306986 [ dbSNP | Ensembl ].
    VAR_052961
    Natural varianti128 – 1281I → T.2 Publications
    Corresponds to variant rs3816873 [ dbSNP | Ensembl ].
    VAR_014017
    Natural varianti166 – 1661N → S.
    Corresponds to variant rs3792683 [ dbSNP | Ensembl ].
    VAR_052962
    Natural varianti168 – 1681V → I Rare polymorphism. 1 Publication
    Corresponds to variant rs61750974 [ dbSNP | Ensembl ].
    VAR_022658
    Natural varianti244 – 2441Q → E.1 Publication
    Corresponds to variant rs17599091 [ dbSNP | Ensembl ].
    VAR_014018
    Natural varianti297 – 2971H → Q.3 Publications
    Corresponds to variant rs2306985 [ dbSNP | Ensembl ].
    VAR_010640
    Natural varianti354 – 3541E → Q.
    Corresponds to variant rs12933 [ dbSNP | Ensembl ].
    VAR_014916
    Natural varianti384 – 3841D → A.1 Publication
    Corresponds to variant rs17029215 [ dbSNP | Ensembl ].
    VAR_010641
    Natural varianti540 – 5401R → H in ABL; loss of activity. 2 Publications
    VAR_010642
    Natural varianti590 – 5901S → I in ABL. 1 Publication
    VAR_010643
    Natural varianti746 – 7461G → E in ABL. 1 Publication
    VAR_010644
    Natural varianti780 – 7801N → Y in ABL; loss of activity. 1 Publication
    VAR_014019

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei134 – 15118EFYSY…NIKRG → GRLDSTTFSPTSYFSSLQ in isoform 2. 1 PublicationVSP_056325Add
    BLAST
    Alternative sequencei152 – 894743Missing in isoform 2. 1 PublicationVSP_056326Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75500 mRNA. Translation: CAA53217.1.
    X59657 mRNA. Translation: CAA42200.1.
    X83013
    , X83014, X83015, X83016, X83017, X83018, X83019, X83020, X83021, X83022, X83023, X83024, X83025, X83026, X83027, X83028, X83029, X83030 Genomic DNA. Translation: CAA58142.1.
    AK290793 mRNA. Translation: BAF83482.1.
    AC083902 Genomic DNA. No translation available.
    BC062696 mRNA. Translation: AAH62696.1.
    BC125110 mRNA. Translation: AAI25111.1.
    BC125111 mRNA. Translation: AAI25112.1.
    CCDSiCCDS3651.1.
    PIRiI38047.
    RefSeqiNP_000244.2. NM_000253.2.
    UniGeneiHs.195799.

    Genome annotation databases

    EnsembliENST00000265517; ENSP00000265517; ENSG00000138823.
    ENST00000422897; ENSP00000407350; ENSG00000138823.
    ENST00000457717; ENSP00000400821; ENSG00000138823.
    GeneIDi4547.
    KEGGihsa:4547.
    UCSCiuc003hvc.4. human.

    Polymorphism databases

    DMDMi1709167.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75500 mRNA. Translation: CAA53217.1 .
    X59657 mRNA. Translation: CAA42200.1 .
    X83013
    , X83014 , X83015 , X83016 , X83017 , X83018 , X83019 , X83020 , X83021 , X83022 , X83023 , X83024 , X83025 , X83026 , X83027 , X83028 , X83029 , X83030 Genomic DNA. Translation: CAA58142.1 .
    AK290793 mRNA. Translation: BAF83482.1 .
    AC083902 Genomic DNA. No translation available.
    BC062696 mRNA. Translation: AAH62696.1 .
    BC125110 mRNA. Translation: AAI25111.1 .
    BC125111 mRNA. Translation: AAI25112.1 .
    CCDSi CCDS3651.1.
    PIRi I38047.
    RefSeqi NP_000244.2. NM_000253.2.
    UniGenei Hs.195799.

    3D structure databases

    ProteinModelPortali P55157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110641. 1 interaction.
    MINTi MINT-1537333.
    STRINGi 9606.ENSP00000265517.

    Chemistry

    BindingDBi P55157.
    ChEMBLi CHEMBL2569.
    DrugBanki DB01094. Hesperetin.

    PTM databases

    PhosphoSitei P55157.

    Polymorphism databases

    DMDMi 1709167.

    Proteomic databases

    MaxQBi P55157.
    PaxDbi P55157.
    PRIDEi P55157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265517 ; ENSP00000265517 ; ENSG00000138823 .
    ENST00000422897 ; ENSP00000407350 ; ENSG00000138823 .
    ENST00000457717 ; ENSP00000400821 ; ENSG00000138823 .
    GeneIDi 4547.
    KEGGi hsa:4547.
    UCSCi uc003hvc.4. human.

    Organism-specific databases

    CTDi 4547.
    GeneCardsi GC04P100485.
    HGNCi HGNC:7467. MTTP.
    HPAi HPA054862.
    MIMi 157147. gene.
    200100. phenotype.
    neXtProti NX_P55157.
    Orphaneti 14. Abetalipoproteinemia.
    426. Familial hypobetalipoproteinemia.
    PharmGKBi PA164742099.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG272516.
    HOGENOMi HOG000113688.
    HOVERGENi HBG006416.
    InParanoidi P55157.
    KOi K14463.
    PhylomeDBi P55157.
    TreeFami TF328754.

    Enzyme and pathway databases

    Reactomei REACT_6841. Chylomicron-mediated lipid transport.

    Miscellaneous databases

    GeneWikii Microsomal_triglyceride_transfer_protein.
    GenomeRNAii 4547.
    NextBioi 17529.
    PROi P55157.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55157.
    Bgeei P55157.
    CleanExi HS_MTTP.
    Genevestigatori P55157.

    Family and domain databases

    Gene3Di 1.25.10.20. 1 hit.
    2.30.230.10. 1 hit.
    InterProi IPR015819. Lipid_transp_b-sht_shell.
    IPR001747. Lipid_transpt_N.
    IPR015816. Vitellinogen_b-sht_N.
    IPR011030. Vitellinogen_superhlx.
    [Graphical view ]
    Pfami PF01347. Vitellogenin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00638. LPD_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48431. SSF48431. 1 hit.
    SSF56968. SSF56968. 1 hit.
    PROSITEi PS51211. VITELLOGENIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein."
      Shoulders C.C., Brett D.J., Bayliss J.D., Narcisi T.M.E., Jarmuz A., Grantham T.T., Leoni P.R.D., Bhattacharya S., Pease R.J., Cullen P.M., Levi S., Byfield P.G.H., Purkiss P., Scott J.
      Hum. Mol. Genet. 2:2109-2116(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    2. "Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemia."
      Sharp D., Blinderman L., Combs K.A., Kienzle B., Ricci B., Wager-Smith K., Gil C.M., Turck C.W., Bouma M.-E., Rader D.J., Aggerbeck L.P., Gregg R.E., Gordon D.A., Wetterau J.R.
      Nature 365:65-69(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Human microsomal triglyceride transfer protein large subunit gene structure."
      Sharp D., Ricci B., Kienzle B., Lin M.C., Wetterau J.R.
      Biochemistry 33:9057-9061(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Blood vessel.
    7. "Transcriptional regulation of human and hamster microsomal triglyceride transfer protein genes. Cell type-specific expression and response to metabolic regulators."
      Hagan D.L., Kienzle B., Jamil H., Hariharan N.
      J. Biol. Chem. 269:28737-28744(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    8. "The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an alpha-helical domain."
      Shoulders C.C., Narcisi T.M.E., Read J., Chester S.A., Brett D.J., Scott J., Anderson T.A., Levitt D.G., Banaszak L.J.
      Nat. Struct. Biol. 1:285-286(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO VITELLOGENINS.
    9. "Mutations of the microsomal triglyceride-transfer-protein gene in abetalipoproteinemia."
      Narcisi T.M.E., Shoulders C.C., Chester S.A., Read J., Brett D.J., Harrison G.B., Grantham T.T., Fox M.F., Povey S., de Bruin T.W.A., Erkelens D.W., Muller D.P.R., Lloyd J.K., Scott J.
      Am. J. Hum. Genet. 57:1298-1310(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-878.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triglyceride transfer protein that prevents complex formation with protein disulfide isomerase."
      Rehberg E.F., Samson-Bouma M.-E., Kienzle B., Blinderman L., Jamil H., Wetterau J.R., Aggerbeck L.P., Gordon D.A.
      J. Biol. Chem. 271:29945-29952(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ABL HIS-540, VARIANTS GLN-297 AND ALA-384, MUTAGENESIS OF ARG-540.
    12. "Microsomal triglyceride transfer protein (MTP) gene mutations in Canadian subjects with abetalipoproteinemia."
      Wang J., Hegele R.A.
      Hum. Mutat. 15:294-295(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ABL HIS-540; ILE-590 AND GLU-746.
    13. "Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia."
      Ohashi K., Ishibashi S., Osuga J., Tozawa R., Harada K., Yahagi N., Shionoiri F., Iizuka Y., Tamura Y., Nagai R., Illingworth D.R., Gotoda T., Yamada N.
      J. Lipid Res. 41:1199-1204(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ABL TYR-780.
    14. "Variants of the microsomal triglyceride transfer protein gene are associated with plasma cholesterol levels and body mass index."
      Ledmyr H., Karpe F., Lundahl B., McKinnon M., Skoglund-Andersson C., Ehrenborg E.
      J. Lipid Res. 43:51-58(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIS-95; THR-128; GLU-244 AND GLN-297.
    15. "Hypobetalipoproteinemia with an apparently recessive inheritance due to a 'de novo' mutation of apolipoprotein B."
      Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L., Bertolini S., Calandra S., Tarugi P.
      Biochim. Biophys. Acta 1688:61-67(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-128; ILE-168 AND GLN-297.

    Entry informationi

    Entry nameiMTP_HUMAN
    AccessioniPrimary (citable) accession number: P55157
    Secondary accession number(s): A8K428, Q08AM4, Q6P5T3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3